ID Q1YDX4_AURMS Unreviewed; 367 AA. AC Q1YDX4; DT 02-MAY-2006, integrated into UniProtKB/TrEMBL. DT 02-MAY-2006, sequence version 1. DT 03-MAY-2023, entry version 81. DE RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000256|HAMAP-Rule:MF_01445}; DE EC=2.3.1.234 {ECO:0000256|HAMAP-Rule:MF_01445}; DE AltName: Full=N6-L-threonylcarbamoyladenine synthase {ECO:0000256|HAMAP-Rule:MF_01445}; DE Short=t(6)A synthase {ECO:0000256|HAMAP-Rule:MF_01445}; DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000256|HAMAP-Rule:MF_01445}; DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein TsaD {ECO:0000256|HAMAP-Rule:MF_01445}; GN Name=tsaD {ECO:0000256|HAMAP-Rule:MF_01445}; GN ORFNames=SI859A1_03651 {ECO:0000313|EMBL:EAS48484.1}; OS Aurantimonas manganoxydans (strain ATCC BAA-1229 / DSM 21871 / SI85-9A1). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Aurantimonadaceae; Aurantimonas. OX NCBI_TaxID=287752 {ECO:0000313|EMBL:EAS48484.1, ECO:0000313|Proteomes:UP000000321}; RN [1] {ECO:0000313|EMBL:EAS48484.1, ECO:0000313|Proteomes:UP000000321} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SI85-9A1 {ECO:0000313|EMBL:EAS48484.1, RC ECO:0000313|Proteomes:UP000000321}; RX PubMed=18344346; DOI=10.1128/AEM.01656-07; RA Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., Bernier-Latmani R., RA McCarthy J.K., Torpey J.W., Clement B.G., Gaasterland T., Tebo B.M.; RT "Genomic insights into Mn(II) oxidation by the marine alphaproteobacterium RT Aurantimonas sp. strain SI85-9A1."; RL Appl. Environ. Microbiol. 74:2646-2658(2008). CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group on CC adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning CC with adenine. Is involved in the transfer of the threonylcarbamoyl CC moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, CC together with TsaE and TsaB. TsaD likely plays a direct catalytic role CC in this reaction. {ECO:0000256|HAMAP-Rule:MF_01445}. CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + CC H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA; CC Xref=Rhea:RHEA:37059, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10163, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:73682, ChEBI:CHEBI:74411, CC ChEBI:CHEBI:74418, ChEBI:CHEBI:456215; EC=2.3.1.234; CC Evidence={ECO:0000256|ARBA:ARBA00001866, ECO:0000256|HAMAP- CC Rule:MF_01445}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01445}; CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01445}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01445}. CC -!- SIMILARITY: Belongs to the KAE1 / TsaD family. {ECO:0000256|HAMAP- CC Rule:MF_01445}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EAS48484.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAPJ01000010; EAS48484.1; -; Genomic_DNA. DR AlphaFoldDB; Q1YDX4; -. DR HOGENOM; CLU_023208_0_2_5; -. DR BioCyc; AURANTIMONAS:SI859A1_03651-MON; -. DR Proteomes; UP000000321; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.420.40; -; 2. DR HAMAP; MF_01445; TsaD; 1. DR InterPro; IPR043129; ATPase_NBD. DR InterPro; IPR000905; Gcp-like_dom. DR InterPro; IPR017861; KAE1/TsaD. DR InterPro; IPR022450; TsaD. DR PANTHER; PTHR11735; TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE; 1. DR PANTHER; PTHR11735:SF6; TRNA N6-ADENOSINE THREONYLCARBAMOYLTRANSFERASE, MITOCHONDRIAL-RELATED; 1. DR Pfam; PF00814; TsaD; 1. DR PRINTS; PR00789; OSIALOPTASE. DR SUPFAM; SSF53067; Actin-like ATPase domain; 1. DR TIGRFAMs; TIGR00329; gcp_kae1; 1. DR TIGRFAMs; TIGR03723; T6A_TsaD_YgjD; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP- KW Rule:MF_01445}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01445}; KW Iron {ECO:0000256|HAMAP-Rule:MF_01445}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01445}; Reference proteome {ECO:0000313|Proteomes:UP000000321}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01445}; KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP- KW Rule:MF_01445}. FT DOMAIN 36..326 FT /note="Gcp-like" FT /evidence="ECO:0000259|Pfam:PF00814" FT BINDING 123 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01445" FT BINDING 127 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01445" FT BINDING 145..149 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01445" FT BINDING 178 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01445" FT BINDING 191 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01445" FT BINDING 195 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01445" FT BINDING 291 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01445" FT BINDING 319 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01445" SQ SEQUENCE 367 AA; 37990 MW; 110BFAFE5862144F CRC64; MTPANPPRPL ILGIETSCDE TAASVVGRDD AGAPVIHSNV VLSQVEEHAA FGGVVPEIAA RAHVEALDGI VKAAMDEAGI GFDELSAVAA TTGPGLVGGL IVGAMTGKAI AAARRLPFLA INHLEGHALT PRLTDRLAYP YLLLLVSGGH SQIVLVRGLG AYERWGTTID DALGEAFDKT AKLLGLPNPG GPHVERRAAA GDPKRFALPR PMKGNPRLDF SFSGLKTALR MAAQAAAPLS PTDVDDLCAG FQAAAADSLA DRVGRALTQF RDRFPDLADP VLAVAGGVAA NRAIRTALEA QTARTGVRLV APPLALCTDN AAMIAYAGLE RFEAGMVDGL DAPVRSRWPL DGDSAPMIGF GRRGAKA //